NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pone.0001450; PubMed=18197260 [NCBI, ExPASy, EBI, Israel, Japan]
Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W., Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T., Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S., Zhao G.-P., Chen H.;
"Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of serotype 3 prevalent in China.";
PLoS ONE 3:E1450-E1450(2008).

Comments

FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) (By similarity).
CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H₂O + O₂ = pyridoxal 5'-phosphate + NH₃ + H₂O₂.
CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O₂ = pyridoxal 5'-phosphate + H₂O₂.
COFACTOR: Binds 1 FMN per subunit (By similarity).
PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1 .
PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1 .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000687; ABY70604.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001653048.1; -.

3D structure databases

ModBase

B0BU37.

Ontologies

GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from HAMAP).
GO:0004733;	Molecular function: pyridoxamine-phosphate oxidase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01629; -; 1.
PBIL [Tree]

InterPro

IPR000659; Pyridox_oxidase.
IPR012349; Split_barrel_FMN_bd.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.110.10; PNPOx_FMN_bd; 1.

PANTHER

PTHR10851; Pyridox_oxidase; 1.

ProDom

PD006312; Pyridox_oxidase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00558; pdxH; 1.

PROSITE

PS01064; PYRIDOX_OXIDASE; 1.

Genome annotation databases

GeneID

5851698; -.

GenomeReviews

CP000687_GR; APJL_2059.

KEGG

apj:APJL_2059; -.

CMR

B0BU37; APJL_2059.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Flavoprotein; FMN; Oxidoreductase; Pyridoxine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 209`	`209`	`Pyridoxine/pyridoxamine 5'-phosphate oxidase.`	`PRO_0000335777`
`NP_BIND`	`74 75`	`2`	`FMN (By similarity).`
`NP_BIND`	`138 139`	`2`	`FMN (By similarity).`
`REGION`	`7 10`	`4`	`Substrate binding (By similarity).`
`REGION`	`188 190`	`3`	`Substrate binding (By similarity).`
`BINDING`	`59 59`		`FMN (By similarity).`
`BINDING`	`62 62`		`FMN; via amide nitrogen (By similarity).`
`BINDING`	`64 64`		`Substrate (By similarity).`
`BINDING`	`81 81`		`FMN (By similarity).`
`BINDING`	`121 121`		`Substrate (By similarity).`
`BINDING`	`125 125`		`Substrate (By similarity).`
`BINDING`	`129 129`		`Substrate (By similarity).`

Sequence information

Length: 209 AA [This is the length of the unprocessed precursor]

Molecular weight: 24022 Da [This is the MW of the unprocessed precursor]

CRC64: 54E1B3808FFEE653 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDLHNIREDY SKQELSQAHC HADPIQQFEQ WLEEAITAKA NEPTAMNVAT VLDGKPTSRI 

        70         80         90        100        110        120 
VLLKEVNPNG FVFFTNYQSR KGQAIEQNPY AALTFFWAEL ERSVRIEGRI EKISAEESDR 

       130        140        150        160        170        180 
YFASRPYTSR VGAWASNQSQ VLSGKSELVA KAALIAAKHP LHVPRPPHWG GYIVLPERIE 

       190        200 
FWQGRPSRLH DRICYRLVEG KWHKERLSP

B0BU37 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools